Protein 4.1: its association with the human erythrocyte membrane.
Protein 4.1: its association with the human erythrocyte membrane.
复制标题
蛋白质 4.1：其与人红细胞膜的关联。
DOI：
10.1073/pnas.81.14.4404
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发表时间：
1984
影响因子：
11.1
通讯作者：
Goodman,SR
中科院分区：
文献类型：
--
作者：
Shiffer,KA;Goodman,SR
125 I标记的蛋白4.1a和4.1b具有与除了其他外周膜蛋白外还耗尽蛋白4.1的由内而外的红细胞囊泡重新结合的同等能力。在4 ℃下，125 I标记的蛋白4.1与蛋白4.1耗尽的囊泡的再结合是盐依赖性的、pH依赖性的，并且是可饱和的，Kd为42-50 nM，外推的最大结合能力为每mg囊泡蛋白结合120-140微克蛋白4.1或每mg鬼蛋白结合60-70微克蛋白4.1，与红细胞膜中的蛋白4.1含量（占总膜蛋白的6-7%）相关。这些囊泡与木瓜蛋白酶（5微克/毫升，4 ℃）的选择性蛋白水解裂解消除了大于60%的高亲和力结合位点，因此，我们得出结论，蛋白4.1与细胞质膜表面的相互作用是通过一个特定的高亲和力蛋白质-蛋白质协会。
125I-labeled protein 4.1a and 4.1b have equal ability to reassociate with inside-out erythrocyte vesicles that were depleted of protein 4.1 in addition to other peripheral membrane proteins. The reassociation of 125I-labeled protein 4.1 to protein 4.1-depleted vesicles at 4 degrees C is salt dependent, pH dependent, and saturable with a Kd of 42-50 nM and an extrapolated maximal binding capacity of 120-140 micrograms of protein 4.1 bound per mg of vesicle protein or 60-70 micrograms of protein 4.1 bound per mg of ghost protein, correlating with the protein 4.1 content in the erythrocyte membrane (6-7% of the total membrane protein). Selective proteolytic cleavage of these vesicles with papain (5 micrograms/ml at 4 degrees C) eliminates greater than 60% of the high-affinity binding sites; therefore, we conclude that the interaction of protein 4.1 with the cytoplasmic membrane surface is through a specific high-affinity protein-protein association.